ID A0A1G2QN44_9BACT Unreviewed; 502 AA.
AC A0A1G2QN44;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN ORFNames=A2117_01925 {ECO:0000313|EMBL:OHA62025.1};
OS Candidatus Wildermuthbacteria bacterium GWA2_46_15.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802443 {ECO:0000313|EMBL:OHA62025.1, ECO:0000313|Proteomes:UP000179245};
RN [1] {ECO:0000313|EMBL:OHA62025.1, ECO:0000313|Proteomes:UP000179245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000256|RuleBase:RU000644}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHA62025.1}.
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DR EMBL; MHTO01000022; OHA62025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QN44; -.
DR STRING; 1802443.A2117_01925; -.
DR Proteomes; UP000179245; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 15..183
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 502 AA; 54766 MW; 973B486CABA14458 CRC64;
MVEKDKQKEN ILTIPRPPIV VVLGHVDSGK TSLLDAVRKS HVAEKESGGI TQHVGAYEVE
FNEKKITFID TPGHEAFSAM RSRGAKVADI AILVIDSVSG IQPQTKEAIG HIKKSGIGLI
VALNKIDLPG ANPERIKQEL IKEGISVESF GGQIPAVEVS AKTGQGLDNL LELILLIAEM
ENLKGDPSQA AEGVVIEAYL DNLKGPLATL LLRDGSLGIG DIIATSTAGG KIKNMEDFRH
QPLTIALPSM PVVVLGLEGV PQVGDKISVF PTMEEARVYL QKKEKKSGEG QVIFIEEGKK
VLNLILKADV SGSLEAIEEV LSGLPQEKVI LRILGKEVGE INESDVKLAE ASKAAILGFR
VKVNLTATIL KERAKVRILS FDIIYTLAQG VRQVMENLLQ PEVEKKILGK LKVLALFLNE
KNRQIIGGKI IEGEIKKGSK LEVWRKDQNV GRGKIISLQE NKKEVFQASR GRECGILFEG
EVKIEEEDIL EAFEEERHKA EL
//
